ID BUR1_GIBZE Reviewed; 539 AA. AC Q4I5U9; A0A0E0SBS4; I1RTA8; DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot. DT 31-OCT-2012, sequence version 2. DT 27-MAR-2024, entry version 112. DE RecName: Full=Serine/threonine-protein kinase BUR1; DE EC=2.7.11.22; DE EC=2.7.11.23; GN Name=BUR1; ORFNames=FGRRES_16828, FGSG_07409; OS Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 OS / PH-1) (Wheat head blight fungus) (Fusarium graminearum). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes; OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium. OX NCBI_TaxID=229533; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1; RX PubMed=17823352; DOI=10.1126/science.1143708; RA Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G., Di Pietro A., RA Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G., Antoniw J., Baldwin T., RA Calvo S.E., Chang Y.-L., DeCaprio D., Gale L.R., Gnerre S., Goswami R.S., RA Hammond-Kosack K., Harris L.J., Hilburn K., Kennell J.C., Kroken S., RA Magnuson J.K., Mannhaupt G., Mauceli E.W., Mewes H.-W., Mitterbauer R., RA Muehlbauer G., Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T., RA Qi W., Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M., RA Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C.; RT "The Fusarium graminearum genome reveals a link between localized RT polymorphism and pathogen specialization."; RL Science 317:1400-1402(2007). RN [2] RP GENOME REANNOTATION. RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1; RX PubMed=20237561; DOI=10.1038/nature08850; RA Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.-J., RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B., RA Houterman P.M., Kang S., Shim W.-B., Woloshuk C., Xie X., Xu J.-R., RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W., RA Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.J., RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E., RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M., RA Kumar L., Lee Y.-H., Li L., Manners J.M., Miranda-Saavedra D., RA Mukherjee M., Park G., Park J., Park S.-Y., Proctor R.H., Regev A., RA Ruiz-Roldan M.C., Sain D., Sakthikumar S., Sykes S., Schwartz D.C., RA Turgeon B.G., Wapinski I., Yoder O., Young S., Zeng Q., Zhou S., RA Galagan J., Cuomo C.A., Kistler H.C., Rep M.; RT "Comparative genomics reveals mobile pathogenicity chromosomes in RT Fusarium."; RL Nature 464:367-373(2010). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1; RX PubMed=26198851; DOI=10.1186/s12864-015-1756-1; RA King R., Urban M., Hammond-Kosack M.C.U., Hassani-Pak K., RA Hammond-Kosack K.E.; RT "The completed genome sequence of the pathogenic ascomycete fungus Fusarium RT graminearum."; RL BMC Genomics 16:544-544(2015). CC -!- FUNCTION: Serine/threonine-protein kinase involved in transcription CC regulation. Phosphorylates the UBC2/RAD6 ubiquitin-conjugating enzyme CC (E2), leading to monoubiquitination of histone H2B and the silencing of CC telomeric-associated genes. Also required for histone H3 methylation. CC Necessary for the recovery from pheromone-induced growth arrest in the CC cell cycle G1 phase (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl- CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA- CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.22; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L- CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; CC EC=2.7.11.22; CC -!- CATALYTIC ACTIVITY: CC Reaction=[DNA-directed RNA polymerase] + ATP = ADP + H(+) + phospho- CC [DNA-directed RNA polymerase]; Xref=Rhea:RHEA:10216, Rhea:RHEA- CC COMP:11321, Rhea:RHEA-COMP:11322, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43176, ChEBI:CHEBI:68546, CC ChEBI:CHEBI:456216; EC=2.7.11.23; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr CC protein kinase family. CDC2/CDKX subfamily. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=ESU13671.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; DS231666; ESU13671.1; ALT_SEQ; Genomic_DNA. DR EMBL; HG970335; CEF83887.1; -; Genomic_DNA. DR RefSeq; XP_011327178.1; XM_011328876.1. DR AlphaFoldDB; Q4I5U9; -. DR SMR; Q4I5U9; -. DR STRING; 229533.Q4I5U9; -. DR GeneID; 23554487; -. DR KEGG; fgr:FGSG_07409; -. DR VEuPathDB; FungiDB:FGRAMPH1_01G24753; -. DR eggNOG; KOG0600; Eukaryota. DR HOGENOM; CLU_000288_181_21_1; -. DR InParanoid; Q4I5U9; -. DR OrthoDB; 10753at2759; -. DR PHI-base; PHI:1231; -. DR PHI-base; PHI:1492; -. DR Proteomes; UP000070720; Chromosome 4. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA. DR GO; GO:0008353; F:RNA polymerase II CTD heptapeptide repeat kinase activity; IEA:UniProtKB-EC. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR CDD; cd07866; STKc_BUR1; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR PANTHER; PTHR24056; CELL DIVISION PROTEIN KINASE; 1. DR PANTHER; PTHR24056:SF584; SERINE_THREONINE-PROTEIN KINASE BUR1; 1. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. PE 3: Inferred from homology; KW ATP-binding; Kinase; Nucleotide-binding; Nucleus; Reference proteome; KW Serine/threonine-protein kinase; Transferase. FT CHAIN 1..539 FT /note="Serine/threonine-protein kinase BUR1" FT /id="PRO_0000085683" FT DOMAIN 37..339 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT REGION 1..27 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 370..539 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 471..539 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 169 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10027" FT BINDING 43..51 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 66 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" SQ SEQUENCE 539 AA; 61614 MW; 1320870273F2BD61 CRC64; MEKLSETTPN GTSPRTFALN HSRPRSSFKG CSRISDYELL GKLGEGTFGE VHRARLRKTG ALVALKKIIM HHEKDGFPIT ALREIKLLKL LSHKNILRLE DMAIEHPTRQ TDKRKKPIVY MATPYMDHDL SGLLDNPSVQ FKEPQIKCYM LQLLEGLRYL HDSRILHRDM KAANLLINNK GILQIADFGL ARHYDGRTPE SGVPMGEGKR DYTGLVVTRW YRPPELLLQL RQYTPAIDVW GVGCVFGEML YGKPILAGES DAAQLDIIWD LMGSPNEENM PRWKSLPGAD HLTPRPRTGN LETRFRQYGS GAVSLLKELL RLDWRTRINA VDALQHPWFK MQPLPLEPHE IPTYEESHEL DRRKFHDRKA ALPPAPKGGT VGVGPDANGA TAGFNSNEPY GNGRNGVNGG RYRNGPDDRR PAWQRERGAG LPPRPPPNND DADFRERGPP RARGPPGPRG PDVDTYIPAY NRDDPGRRRD DRPPPPRDDR PPPRDDRRRR NSREDRRFDR DRGTMSRSRS PRHDRSRDRD RPDHNGYRR //